|Other Names||Neprilysin, Atriopeptidase, Common acute lymphocytic leukemia antigen, CALLA, Enkephalinase, Neutral endopeptidase 2411, NEP, Neutral endopeptidase, Skin fibroblast elastase, SFE, CD10, MME, EPN|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7329c was selected from the Center region of human MME. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in the degradation of atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573).|
|Cellular Location||Cell membrane; Single-pass type II membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
MME is a common acute lymphocytic leukemia antigen that is an important cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). This protein is present on leukemic cells of pre-B phenotype, which represent 85% of cases of ALL. This protein is not restricted to leukemic cells, however, and is found on a variety of normal tissues. It is a oprotein that is particularly abundant in kidney, where it is present on the brush border of proximal tubules and on glomerular epithelium. The protein is a neutral endopeptidase that cleaves peptides at the amino side of hydrophobic residues and inactivates several peptide hormones including glucagon, enkephalins, substance P, neurotensin, oxytocin, and bradykinin.
Dakka,N., Bellaoui,H. Pediatr Hematol Oncol 26 (4), 216-231 (2009)Wang,R., Wang,S. J. Neurochem. 108 (4), 1072-1082 (2009)Shipp,M.A. Proc. Natl. Acad. Sci. U.S.A. 88 (23), 10662-10666 (1991)Shipp,M.A. Proc. Natl. Acad. Sci. U.S.A. 86 (1), 297-301 (1989)
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